Purification, characterization and therm
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Anil Kumar Singh; Hari S. Chhatpar
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Article
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2011
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John Wiley and Sons
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English
β 345 KB
A 20 kDa antifungal serine protease from Streptomyces sp. A6 was purified to 34.56 folds by gel permeation chromatography. The enzyme exhibited highest activity at neutral to near alka- line pH 7-9 and 55 Β°C. Neutral surfactant triton X-100 enhanced the activity by 4.12 fold. The protease activity a